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Extra resources for ADME and Translational Pharmacokinetics / Pharmacodynamics of Therapeutic Proteins: Applications in Drug Discovery and Development

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The domain structure of the antibody molecule also lends itself to other engineered formats designed to achieve new modalities, such as bispecificity. Several approaches have been taken to promote heavy‐ chain heterodimer formation, including a “knobs into holes” method [79] and a method exploiting the phenomenon of Fab‐arm exchange [80]. Other approaches aim to combine IgG with additional smaller antigen‐binding fragments fused to the C‐terminus of heavy or light chain [81]. It is beyond the scope of this chapter to describe in full this plethora of bispecific strategies, but they do serve to highlight the power of protein engineering techniques to create Ig‐based novel molecules to achieve new therapeutic modalities.

These include the Ser‐239 to Asp, Isoleucine (Ile)‐332 to Glu changes that offer significant improvements in ADCC [72], plus the Ser‐267 to Glu, Histidine (His)‐268 to Ser, Ser‐324 to Thr combination to improve CDC [73]. In addition, since glycosylation at Asn‐297 is critical for Fc structure and effector function, glycoengineering has been undertaken to enhance activity [74]. 1), which have shown success in the clinic and offer even greater future potential. The simplest is the Fab fragment that offers monovalent antigen binding without any Fc‐mediated effector function.